Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors-Reference-Cited by-同舟云学术

Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors

Published:2017-09-14 Issue:18 Volume:60 Page:7863-7875
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Zhu Jin-Yi¹,Cuellar Rebecca A.²,Berndt Norbert¹,Lee Hee Eun¹,Olesen Sanne H.¹,Martin Mathew P.¹,Jensen Jeffrey T.³,Georg Gunda I.²^ORCID,Schönbrunn Ernst¹^ORCID

Affiliation:

1. Drug Discovery Department, Moffitt Cancer Center, Tampa, Florida 33612, United States

2. Department of Medicinal Chemistry, University of Minnesota, Minneapolis, Minnesota 55414, United States

3. Division of Reproductive and Developmental Science, Oregon National Primate Research Center, Beaverton, Oregon 97006, United States

Funder

National Institute of Child Health and Human Development

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.7b00996

Reference47 articles.

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2. mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of cdc2

3. Inactivation of the p34cdc2-cyclin B complex by the human WEE1 tyrosine kinase

4. Cell-cycle checkpoints and cancer

5. G2 checkpoint abrogation and checkpoint kinase-1 targeting in the treatment of cancer

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